Evidence map›Paper›PMID 26070108›Full record

ReviewCurrent opinion in immunology2015

Novel antigens for RSV vaccines.

Barney S Graham, Kayvon Modjarrad, Jason S McLellan

Registry-linked trialAbstract readReview
In one paragraph

Review in Current opinion in immunology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT03049488 (VRC 317), which is not on this map. Cited by 100 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed, 3 pooled it
8.7field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

NCT03049488 phase1completednot on this mapstarted 2017, after this paper: background citation

VRC 317: A Phase I Randomized, Open-Label Clinical Trial to Evaluate Dose, Safety, Tolerability and Immunogenicity of a Stabilized Prefusion RSV F Subunit Protein Vaccine, VRC-RSVRGP084-00-VP (DS-Cav1), Alone or With Alum Adjuvant, in Healthy Adults

TypeinterventionalSponsorNational Institute of Allergy and Infectious Diseases (NIAID)Ran2017 to 2019Enrolled95ConditionsRespiratory Syncytial VirusArmsVRC-RSVRGP084-00-VP, Aluminum Hydroxide Suspension
3 · Its place in the literature

Who cites it

100 citing papers in PubMed, 3 syntheses or guidelines pooled it, 144 citations in OpenAlex.

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40 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 3 institutions in 1 country.

Barney S GrahamVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: bgraham@nih.gov.
Kayvon ModjarradU.S. Military HIV Research Program, Walter Reed Army Institute of Research, Silver Spring, MD, USA; Henry M. Jackson Foundation for the Advancement of Military Medicine, Bethesda, MD, USA.
Jason S McLellanDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, 7200 Vail, Hanover, NH 03755, USA.
Dartmouth College · USNational Institutes of Health · USWalter Reed Army Institute of Research · US

Funding

Antigenicity and Immunogenicity of Stabilized prefusion F proteinZIAAI005129 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI GRAHAM, BARNEY · 2016 to 2021
$7.9M
Vectors and Methods to Increase Immunogenicity during DNA VaccinationZIAAI005061 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI GRAHAM, BARNEY · 2009 to 2017
$7.7M
Dityrosine Locked Prefusion F Protein: A Path To A Protective RSV VaccineR43AI112124 · NIAID · AVATAR MEDICAL, LLC · PI MCLELLAN, JASON SCOTT, YONDOLA, MARK · 2014 to 2015
$596k
Intramural NIH HHS Z99 AI999999NIAID NIH HHS 1R43AI112124NIAID NIH HHS R43 AI112124
6 · The paper itself

Abstract

Respiratory syncytial virus (RSV) remains a leading global cause of infant mortality and adult morbidity. Infection, which recurs throughout life, elicits only short-lived immunity. The development of a safe and efficacious vaccine has, thus far, been elusive. Recent technological advances, however, have yielded promising RSV vaccine candidates that are based on solving atomic-level structures of surface glycoproteins interacting with neutralizing antibodies. The class I fusion glycoprotein, F, serves as the primary antigenic component of most vaccines, and is the target of the only licensed monoclonal antibody product used to reduce the frequency of severe disease in high-risk neonates. However, success of prior F-based vaccines has been limited by the lack of understanding how the conformational rearrangement between a metastable prefusion F (pre-F) and a stable postfusion F (post-F) affected the epitope content. Neutralizing epitopes reside on both conformations, but those specific to pre-F are far more potent than those previously identified and present on post-F. The solution of the pre-F structure and its subsequent characterization and stabilization illustrates the value of a structure-based approach to vaccine development, and provides hope that a safe and effective RSV vaccine is possible.

Indexed as

AnimalsAntibodies, NeutralizingEpitopes, B-LymphocyteHumansImmunityInfant, NewbornProtein ConformationRespiratory Syncytial VirusesRespiratory Syncytial Virus InfectionsRespiratory Syncytial Virus VaccinesStructure-Activity RelationshipViral Fusion ProteinsAntibodies, NeutralizingEpitopes, B-LymphocyteRespiratory Syncytial Virus VaccinesViral Fusion Proteins

Identifiers

PMID26070108
PMCPMC4553118
OpenAlexW617135685

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.